ID   DCAM1_BRAJU             Reviewed;         368 AA.
AC   Q42613;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 56.
DE   RecName: Full=S-adenosylmethionine decarboxylase proenzyme 1;
DE            Short=AdoMetDC 1;
DE            Short=SAMDC 1;
DE            EC=4.1.1.50;
DE   Contains:
DE     RecName: Full=S-adenosylmethionine decarboxylase 1 alpha chain;
DE   Contains:
DE     RecName: Full=S-adenosylmethionine decarboxylase 1 beta chain;
DE   Flags: Precursor;
GN   Name=SAMDC1;
OS   Brassica juncea (Leaf mustard) (Indian mustard).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Brassica.
OX   NCBI_TaxID=3707;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Lee T., Liu J.-J., Pua E.-C.;
RT   "Molecular cloning of two cDNAs encoding S-adenosyl-L-methionine
RT   decarboxylase in mustard (Brassica juncea [L.] Czern & Coss).";
RL   (er) Plant Gene Register PGR97-157.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine = (5-deoxy-5-
CC       adenosyl)(3-aminopropyl)-methylsulfonium salt + CO(2).
CC   -!- COFACTOR: Pyruvoyl group (By similarity).
CC   -!- PATHWAY: Amine and polyamine biosynthesis; S-
CC       adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from
CC       S-adenosyl-L-methionine: step 1/1.
CC   -!- PTM: Is synthesized initially as an inactive proenzyme. Formation
CC       of the active enzyme involves a self-maturation process in which
CC       the active site pyruvoyl group is generated from an internal
CC       serine residue via an autocatalytic post-translational
CC       modification. Two non-identical subunits are generated from the
CC       proenzyme in this reaction, and the pyruvate is formed at the N-
CC       terminus of the alpha chain, which is derived from the carboxyl
CC       end of the proenzyme. The post-translation cleavage follows an
CC       unusual pathway, termed non-hydrolytic serinolysis, in which the
CC       side chain hydroxyl group of the serine supplies its oxygen atom
CC       to form the C-terminus of the beta chain, while the remainder of
CC       the serine residue undergoes an oxidative deamination to produce
CC       ammonia and the pyruvoyl group blocking the N-terminus of the
CC       alpha chain (By similarity).
CC   -!- SIMILARITY: Belongs to the eukaryotic AdoMetDC family.
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DR   EMBL; X95729; CAA65044.1; -; mRNA.
DR   HSSP; P17707; 1JEN.
DR   BRENDA; 4.1.1.50; 21235.
DR   GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IEA:EC.
DR   GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006597; P:spermine biosynthetic process; IEA:InterPro.
DR   InterPro; IPR001985; S-AdoMet_decarboxylase.
DR   InterPro; IPR018167; S-AdoMet_decarboxylase_sg.
DR   InterPro; IPR016067; S-AdoMet_deCO2ase_core.
DR   InterPro; IPR018166; S-AdoMet_deCO2ase_CS.
DR   Gene3D; G3DSA:3.60.90.10; SAM_decarbox; 1.
DR   PANTHER; PTHR11570; SAM_decarbox; 1.
DR   Pfam; PF01536; SAM_decarbox; 1.
DR   PIRSF; PIRSF001355; S-AdenosylMet_decarboxylase; 1.
DR   ProDom; PD002379; SAM_decarbox; 1.
DR   TIGRFAMs; TIGR00535; SAM_DCase; 1.
DR   PROSITE; PS01336; ADOMETDC; 1.
PE   2: Evidence at transcript level;
KW   Autocatalytic cleavage; Decarboxylase; Lyase; Polyamine biosynthesis;
KW   Pyruvate; S-adenosyl-L-methionine; Schiff base;
KW   Spermidine biosynthesis; Zymogen.
FT   CHAIN         1     68       S-adenosylmethionine decarboxylase 1 beta
FT                                chain (By similarity).
FT                                /FTId=PRO_0000029991.
FT   CHAIN        69    368       S-adenosylmethionine decarboxylase 1
FT                                alpha chain (By similarity).
FT                                /FTId=PRO_0000029992.
FT   ACT_SITE      9      9       By similarity.
FT   ACT_SITE     12     12       By similarity.
FT   ACT_SITE     69     69       Schiff-base intermediate with substrate;
FT                                via pyruvic acid (By similarity).
FT   ACT_SITE     83     83       Proton donor; for catalytic activity (By
FT                                similarity).
FT   ACT_SITE    234    234       Proton acceptor; for processing activity
FT                                (By similarity).
FT   ACT_SITE    247    247       Proton acceptor; for processing activity
FT                                (By similarity).
FT   SITE         68     69       Cleavage (non-hydrolytic); by autolysis
FT                                (By similarity).
FT   MOD_RES      69     69       Pyruvic acid (Ser); by autocatalysis (By
FT                                similarity).
SQ   SEQUENCE   368 AA;  40453 MW;  DC73830213274B05 CRC64;
     MSLSAIGFEG LRERLEVSFF EPSLFLDTHG KGLRALSKSQ IDEILAPAEC TIVSSLSNDE
     LDSYVLSESS LFIFPYKIII KTCGTTKLLL SIEPLLRLAG GVSLEVKSVR YTRGSFLCPG
     GQPFPQRNLS EEVSVLDGHF AKMGLSSVAY LMGDDDETKK WHVYSASAPA KNSNGDNNVY
     TLEMCMSGLD KDKASVFFKN ESSSAGSMTD NSGIRKILPQ SQICDFEFEP CGYSMNSVEG
     DASSTIHVTP EDGFSYASFE AVGYDFTTMD LSQLVSRVLT CFEPKQFSVA VHSSVAQKSY
     DHSGLSVDLE DYGCRETTVG VSRRRERNSD VSEVREAGNV LWFSEIDLKC EWSSNSSCTS
     EDEKEEGI
//